Copper resistance in the cold: Genome analysis and characterisation of a P IB‐1 ATPase in Bizionia argentinensis

Abstract Copper homeostasis is a fundamental process in organisms, characterised by unique pathways that have evolved to meet specific needs while preserving core resistance mechanisms. While these systems are well‐documented in model bacteria, information on copper resistance in species adapted to...

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Bibliographic Details
Published in:Environmental Microbiology Reports
Main Authors: Burgardt, Noelia I., Melian, Noelia A., González Flecha, F. Luis
Other Authors: Fondo para la Investigación Científica y Tecnológica, Consejo Nacional de Investigaciones Científicas y Técnicas, Universidad de Buenos Aires
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 2024
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Online Access:http://dx.doi.org/10.1111/1758-2229.13278
Description
Summary:Abstract Copper homeostasis is a fundamental process in organisms, characterised by unique pathways that have evolved to meet specific needs while preserving core resistance mechanisms. While these systems are well‐documented in model bacteria, information on copper resistance in species adapted to cold environments is scarce. This study investigates the potential genes related to copper homeostasis in the genome of Bizionia argentinensis (JUB59‐T), a psychrotolerant bacterium isolated from Antarctic seawater. We identified several genes encoding proteins analogous to those crucial for copper homeostasis, including three sequences of copper‐transport P1B‐type ATPases. One of these, referred to as BaCopA1, was chosen for cloning and expression in Saccharomyces cerevisiae . BaCopA1 was successfully integrated into yeast membranes and subsequently extracted with detergent. The purified BaCopA1 demonstrated the ability to catalyse ATP hydrolysis at low temperatures. Structural models of various BaCopA1 conformations were generated and compared with mesophilic and thermophilic homologous structures. The significant conservation of critical residues and structural similarity among these proteins suggest a shared reaction mechanism for copper transport. This study is the first to report a psychrotolerant P1B‐ATPase that has been expressed and purified in a functional form.